Journal article
Reducing agent-mediated nonenzymatic conversion of 2‐oxoglutarate to succinate: implications for oxygenase assays
- Abstract:
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l‐Ascorbate (l‐Asc) is often added to assays with isolated FeII‐ and 2‐oxoglutarate (2OG)‐dependent oxygenases to enhance activity. l‐Asc is proposed to be important in catalysis by some 2OG oxygenases in vivo. We report observations on the nonenzymatic conversion of 2OG to succinate, which is mediated by hydrogen peroxide generated by the reaction of l‐Asc and dioxygen. Slow nonenzymatic oxidation of 2OG to succinate occurs with some, but not all, other reducing agents commonly used in 2OG o...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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- Files:
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(Supplementary materials, 3.3MB)
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(Version of record, 954.7KB)
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- Publisher copy:
- 10.1002/cbic.202000185
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Funding
Bibliographic Details
- Publisher:
- Wiley Publisher's website
- Journal:
- ChemBioChem Journal website
- Volume:
- 21
- Issue:
- 20
- Pages:
- 2898-2902
- Publication date:
- 2020-08-18
- Acceptance date:
- 2020-06-01
- DOI:
- EISSN:
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1439-7633
- ISSN:
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1439-4227
Item Description
- Language:
- English
- Keywords:
- Pubs id:
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1107798
- Local pid:
- pubs:1107798
- Deposit date:
- 2020-06-01
Terms of use
- Copyright holder:
- Khan et al.
- Copyright date:
- 2020
- Rights statement:
- © The Authors. 2020 Wiley‐VCH GmbH This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
- Licence:
- CC Attribution (CC BY)
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